Human CX3CL1(1-76) (FRCD, fractalkine chemokine domain) comprises the 76 N-terminal residues of human CX3CL1. Originally known as fractalkine, CX3CL1 is the only chemokine with a CX3C N-terminal dicysteine motif and also contains a long C-terminal extension consisting of a mucin-like stalk attached to a transmembrane domain. CX3CL1 binds the CX3CR1 receptor and can function as a soluble T cell and monocyte chemotattractant, when cleaved from the transmembrane domain, or can promote adhesion of those cells to endothelial surfaces. CX3CL1 is also a ligand for the human cytomegalovirus-encoded G protein-coupled receptor US28. Its dual role as a soluble chemoattractant and membrane-bound adhesion molecule supports immune surveillance, inflammation, and tissue repair, with implications in atherosclerosis, neuroinflammation, and cancer, making it a key target for immunological and therapeutic research.
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